한빛사 논문
Byung-Gil Lee1,11, Fabian Merkel 2,3,11, Matteo Allegretti 4, Markus Hassler 2,5, Christopher Cawood 6, Léa Lecomte 2,3, Francis J. O’Reilly 7, Ludwig R. Sinn 7, Pilar Gutierrez-Escribano6, Marc Kschonsak2,10, Sol Bravo 2, Takanori Nakane 1, Juri Rappsilber 7,8, Luis Aragon6 ,*,Martin Beck 2,4,9,*, Jan Löwe 1,* and Christian H. Haering 2,4,5,*
1 MRC Laboratory of Molecular Biology, Cambridge, UK.
2 Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
3 Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany.
4 Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
5 Biocenter, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.
6 MRC London Institute of Medical Sciences, London, UK.
7 Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
8 Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
9 Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
10 Present address: Structural Biology, Genentech, South San Francisco, CA, USA.
11 These authors contributed equally: Byung-Gil Lee, Fabian Merkel.
*Corresponding author
Abstract
Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities.
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